2PL9
Crystal Structure of CheY-Mg(2+)-BeF(3)(-) in Complex with CheZ(C19) Peptide solved from a P2(1)2(1)2 Crystal
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0000155 | molecular_function | phosphorelay sensor kinase activity |
A | 0000160 | biological_process | phosphorelay signal transduction system |
A | 0005737 | cellular_component | cytoplasm |
A | 0006935 | biological_process | chemotaxis |
A | 0009927 | molecular_function | histidine phosphotransfer kinase activity |
A | 0046872 | molecular_function | metal ion binding |
A | 0097588 | biological_process | archaeal or bacterial-type flagellum-dependent cell motility |
B | 0000155 | molecular_function | phosphorelay sensor kinase activity |
B | 0000160 | biological_process | phosphorelay signal transduction system |
B | 0005737 | cellular_component | cytoplasm |
B | 0006935 | biological_process | chemotaxis |
B | 0009927 | molecular_function | histidine phosphotransfer kinase activity |
B | 0046872 | molecular_function | metal ion binding |
B | 0097588 | biological_process | archaeal or bacterial-type flagellum-dependent cell motility |
C | 0000155 | molecular_function | phosphorelay sensor kinase activity |
C | 0000160 | biological_process | phosphorelay signal transduction system |
C | 0005737 | cellular_component | cytoplasm |
C | 0006935 | biological_process | chemotaxis |
C | 0009927 | molecular_function | histidine phosphotransfer kinase activity |
C | 0046872 | molecular_function | metal ion binding |
C | 0097588 | biological_process | archaeal or bacterial-type flagellum-dependent cell motility |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE MG A 130 |
Chain | Residue |
A | ASP13 |
A | ASP57 |
A | ASN59 |
A | BEF131 |
A | HOH132 |
A | HOH144 |
site_id | AC2 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE MG B 130 |
Chain | Residue |
B | BEF131 |
B | HOH133 |
B | HOH134 |
B | ASP13 |
B | ASP57 |
B | ASN59 |
site_id | AC3 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE MG C 130 |
Chain | Residue |
C | ASP13 |
C | ASP57 |
C | ASN59 |
C | BEF131 |
C | HOH132 |
C | HOH133 |
site_id | AC4 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE BEF A 131 |
Chain | Residue |
A | ASP57 |
A | TRP58 |
A | ASN59 |
A | THR87 |
A | ALA88 |
A | LYS109 |
A | MG130 |
site_id | AC5 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE BEF B 131 |
Chain | Residue |
B | ASP57 |
B | TRP58 |
B | ASN59 |
B | THR87 |
B | ALA88 |
B | LYS109 |
B | MG130 |
B | HOH133 |
site_id | AC6 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE MES B 132 |
Chain | Residue |
B | ASP3 |
C | ASP13 |
C | PHE14 |
C | SER15 |
site_id | AC7 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE BEF C 131 |
Chain | Residue |
C | ASP57 |
C | TRP58 |
C | ASN59 |
C | THR87 |
C | ALA88 |
C | LYS109 |
C | MG130 |
C | HOH132 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 3 |
Details | BINDING: BINDING => ECO:0000250|UniProtKB:A0A0H3AMJ9 |
Chain | Residue | Details |
A | ASP12 | |
B | ASP12 | |
C | ASP12 |
site_id | SWS_FT_FI2 |
Number of Residues | 9 |
Details | BINDING: BINDING => ECO:0000269|PubMed:16674976, ECO:0000269|PubMed:18083806, ECO:0000269|PubMed:8257674, ECO:0007744|PDB:2CHE, ECO:0007744|PDB:2FKA, ECO:0007744|PDB:2FLW, ECO:0007744|PDB:2FMH, ECO:0007744|PDB:2FMK, ECO:0007744|PDB:2PL9, ECO:0007744|PDB:2PMC |
Chain | Residue | Details |
A | ASP13 | |
A | ASP57 | |
A | ASN59 | |
B | ASP13 | |
B | ASP57 | |
B | ASN59 | |
C | ASP13 | |
C | ASP57 | |
C | ASN59 |
site_id | SWS_FT_FI3 |
Number of Residues | 3 |
Details | MOD_RES: 4-aspartylphosphate => ECO:0000255|PROSITE-ProRule:PRU00169, ECO:0000269|PubMed:1902474, ECO:0000269|PubMed:3280143 |
Chain | Residue | Details |
A | ASP57 | |
B | ASP57 | |
C | ASP57 |
site_id | SWS_FT_FI4 |
Number of Residues | 6 |
Details | MOD_RES: N6-acetyllysine => ECO:0000250 |
Chain | Residue | Details |
A | LYS92 | |
A | LYS109 | |
B | LYS92 | |
B | LYS109 | |
C | LYS92 | |
C | LYS109 |